2hnk

Publication Abstract from PubMed

The S-adenosylmethionine (SAM)-dependent O-methyltransferase from Leptospira interrogans (LiOMT) expressed by gene LA0415 belongs to the Methyltransf_3 family (Pfam PF01596). In this family all of the five bacterial homologues with known function are reported as SAM-dependent O-methylstransferases involved in antibiotic production. The crystal structure of LiOMT in complex with S-adenosylhomocysteine reported here is the first bacterial protein structure in this family. The LiOMT structure shows a conserved SAM-binding region and a probable metal-dependent catalytic site. The molecules of LiOMT generate homodimers by N-terminal swapping, which assists the pre-organization of the substrate-binding site. Based on the sequence and structural analysis, it is implied by the catalytic and substrate-binding site that the substrate of LiOMT is a phenolic derivative, which probably has a large ring-shaped moiety.

Crystal structure of SAM-dependent O-methyltransferase from pathogenic bacterium Leptospira interrogans.,Hou X, Wang Y, Zhou Z, Bao S, Lin Y, Gong W J Struct Biol. 2007 Sep;159(3):523-8. Epub 2007 Apr 30. PMID:17561415^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.